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Near‐cognate suppression of amber, opal and quadruplet codons competes with aminoacyl‐tRNA Pyl for genetic code expansion
Author(s) -
O'Donoghue Patrick,
Prat Laure,
Heinemann Ilka U.,
Ling Jiqiang,
Odoi Keturah,
Liu Wenshe R.,
Söll Dieter
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.09.033
Subject(s) - genetic code , amino acid , transfer rna , stop codon , genetics , escherichia coli , biology , cognate , aminoacyl trna synthetase , codon usage bias , amino acyl trna synthetases , gene , genome , rna , linguistics , philosophy
Over 300 amino acids are found in proteins in nature, yet typically only 20 are genetically encoded. Reassigning stop codons and use of quadruplet codons emerged as the main avenues for genetically encoding non‐canonical amino acids (NCAAs). Canonical aminoacyl‐tRNAs with near‐cognate anticodons also read these codons to some extent. This background suppression leads to ‘statistical protein’ that contains some natural amino acid(s) at a site intended for NCAA. We characterize near‐cognate suppression of amber, opal and a quadruplet codon in common Escherichia coli laboratory strains and find that the PylRS/tRNA Pyl orthogonal pair cannot completely outcompete contamination by natural amino acids.